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Threonine (symbol Thr or T) [2] is an amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), a carboxyl group (which is in the deprotonated −COO − form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid.
In case of humans there are 9 EAAs: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. [1] EAAs are provided in both animal and plant-based food. The EAAs in plants vary greatly due to the vast variation in the plant world and, in general, plants have much lower content of proteins than animal ...
Pregnant women with PKU must control their blood phenylalanine levels even if the fetus is heterozygous for the defective gene because the fetus could be adversely affected due to hepatic immaturity. [medical citation needed] A non-food source of phenylalanine is the artificial sweetener aspartame. This compound is metabolized by the body into ...
^a CID 69435 from PubChem (D-Threonine) ^a CID 6288 from PubChem (L-Threonine) This page was last edited on 12 April 2023, at 11:55 (UTC). Text is ...
Spirulina is being investigated to address food security and malnutrition, and as dietary support in long-term space flight or Mars missions. [12] [13] Its advantage for food security is that it needs less land and water than livestock to produce protein and energy. [12]
Protein occurs in a wide range of food. [11] [12] On a worldwide basis, plant protein foods contribute over 60% of the per capita supply of protein. [9] In North America, animal-derived foods contribute about 70% of protein sources. [12] Insects are a source of protein in many parts of the world. [13]
High levels of threonine result in low levels of homoserine synthesis. The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate ...
Threonine proteases use the secondary alcohol of their N-terminal threonine as a nucleophile to perform catalysis. [1] [2] The threonine must be N-terminal since the terminal amine of the same residue acts as a general base by polarising an ordered water which deprotonates the alcohol to increase its reactivity as a nucleophile.